% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Martin:863860,
      author       = {Martin, Remy and Larsen, Andreas Haahr and Corey, Robin
                      Adam and Midtgaard, Søren Roi and Frielinghaus, Henrich and
                      Schaffitzel, Christiane and Arleth, Lise and Collinson, Ian},
      title        = {{S}tructure and {D}ynamics of the {C}entral {L}ipid {P}ool
                      and {P}roteins of the {B}acterial {H}olo-{T}ranslocon},
      journal      = {Biophysical journal},
      volume       = {116},
      number       = {10},
      issn         = {0006-3495},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2019-03831},
      pages        = {1931 - 1940},
      year         = {2019},
      abstract     = {The bacterial Sec translocon, SecYEG, associates with
                      accessory proteins YidC and the SecDF-YajC subcom-plex to
                      form the bacterial holo-translocon (HTL). The HTL is a
                      dynamic and flexible protein transport machine capable of
                      coor-dinating protein secretion across the membrane and
                      efficient lateral insertion of nascent membrane proteins.
                      It has been hypothesized that a central lipid core
                      facilitates the controlled passage of membrane proteins into
                      the bilayer, ensuring the efficient formation of their
                      native state. By performing small-angle neutron scattering
                      on protein solubilized in ‘‘match-out’’ deuterated
                      detergent, we have been able to interrogate a
                      ‘‘naked’’ HTL complex, with the scattering
                      contribution of the sur-rounding detergent micelle rendered
                      invisible. Such an approach has allowed the confirmation of
                      a lipid core within the HTL, which accommodates between 8
                      and 29 lipids. Coarse-grained molecular dynamics simulations
                      of the HTL also demon-strate a dynamic, central pool of
                      lipids. An opening at this lipid-rich region between YidC
                      and the SecY lateral gate may provide an exit gateway for
                      newly synthesized, correctly oriented, membrane protein
                      helices, or even small bundles of helices, to emerge from
                      the HTL.},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31053257},
      UT           = {WOS:000468419300015},
      doi          = {10.1016/j.bpj.2019.04.002},
      url          = {https://juser.fz-juelich.de/record/863860},
}